P81072 (AMPD1_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: AMP deaminase 1 EC=3.5.4.6 Alternative name(s): AMP deaminase isoform M Myoadenylate deaminase | ||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 26 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | AMP deaminase plays a critical role in energy metabolism. |
| Catalytic activity | AMP + H2O = IMP + NH3. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Pathway | Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. |
| Subunit structure | Homotetramer. |
| Tissue specificity | Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes. |
| Sequence similarities | Belongs to the adenosine and AMP deaminases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | AMP deaminase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "AMP-deaminases from chicken and rabbit muscle: partial primary sequences of homologous 17-kDa CNBr fragments: autorecognition by rabbit anti-[chicken AMPD]." Chilson O.P., Kelly-Chilson A.E., Siegel N.R. Comp. Biochem. Physiol. 116B:371-377(1997) [PubMed: 9114497] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P81072. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | maNOG06305. |
| GeneTree | ENSGT00390000008190. |
| OrthoDB | EOG402WRH. |
Family and domain databases | |
| PROSITE | PS00485. A_DEAMINASE. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPD1_RABIT | ||||||||
| Accession | Primary (citable) accession number: P81072 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with